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language
eng
Author
Haroutunian A., V.
Mishima, Koichi
Tanigawa, Yoshinori
Shimoyama, Makoto
Description
We investigated the ADP-ribosylation of AMP-deaminase from rat and rabbit skeletal muscle by guanidino compound-specific ADP-ribosyltransferase from hen liver nuclei and its effect on the enzyme activity. Rat AMP-deaminase was ADP-ribosylated when the enzyme was incubated with ADP-ribosyl-transferase and [adenylate-^32P] NAD. Preincubation of rabbit AMP-deaminase alone resulted in a loss of ADP-dependent, but not basal, enzyme activity. If, however, the enzyme was subjected to the ADP-ribosylation system containing unlabeled NAD and ADP-ribosyltransferase, the enzyme retained the property to be activated by ADP. Electrophoretic analyses of the enzyme preparation incubated with or without the ADP-ribosylation system and subsequently further incubation with trypsin showed that the ADP-ribosylation of the enzyme protects the enzyme from proteolysis concomitant with the retention of ADP-dependent activation of the enzyme.
Subject
ADP-ribose
AMP-deaminase
regulation
Journal Title
Shimane journal of medical science
Volume
11
Start Page
1
End Page
12
ISSN
03865959
ISSN(Online)
24332410
Published Date
1988
NCID
AA00841586
Publisher Aalternative
Shimane Medical University
NII Type
Departmental Bulletin Paper
Format
PDF
Text Version
出版社版
Gyoseki ID
e28126
OAI-PMH Set
Faculty of Medicine
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